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Conserved domains on  [gi|1343871178|ref|NP_001347742|]
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ergosterol biosynthetic protein 28 homolog isoform 2 [Mus musculus]

Protein Classification

Erg28 family protein( domain architecture ID 10508604)

Erg28 family protein similar to Saccharomyces cerevisiae ergosterol biosynthetic protein 28 (Erg28) that functions as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum, and may also be responsible for facilitating their interaction

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Erg28 pfam03694
Erg28 like protein; This is a family of integral membrane proteins, which may contain four ...
8-75 7.04e-26

Erg28 like protein; This is a family of integral membrane proteins, which may contain four transmembrane helices. Members of this family are thought to be involved in sterol C-4 demethylation. In S. cerevisiae they may tether Erg26p (sterol dehydrogenase/decarboxylase) and Erg27p (3-ketoreductase) to the endoplasmic reticulum or may facilitate interaction between these proteins. The family contains a conserved arginine and histidine that may be functionally important.


:

Pssm-ID: 461015  Cd Length: 111  Bit Score: 91.79  E-value: 7.04e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343871178   8 LRSWLVMVSIIAMGNTLQSFRdHTFLYEKLYTGKPNLVNGLQARTFGIWTLLSSVIRCLCAIDIHNKT 75
Cdd:pfam03694   1 LPYWLLFVSVVALGNSVQNYF-TLFLTRRVYSGKPKQVTPLSARTFGTWTLLSAIIRLYAAYNIHNKP 67
 
Name Accession Description Interval E-value
Erg28 pfam03694
Erg28 like protein; This is a family of integral membrane proteins, which may contain four ...
8-75 7.04e-26

Erg28 like protein; This is a family of integral membrane proteins, which may contain four transmembrane helices. Members of this family are thought to be involved in sterol C-4 demethylation. In S. cerevisiae they may tether Erg26p (sterol dehydrogenase/decarboxylase) and Erg27p (3-ketoreductase) to the endoplasmic reticulum or may facilitate interaction between these proteins. The family contains a conserved arginine and histidine that may be functionally important.


Pssm-ID: 461015  Cd Length: 111  Bit Score: 91.79  E-value: 7.04e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343871178   8 LRSWLVMVSIIAMGNTLQSFRdHTFLYEKLYTGKPNLVNGLQARTFGIWTLLSSVIRCLCAIDIHNKT 75
Cdd:pfam03694   1 LPYWLLFVSVVALGNSVQNYF-TLFLTRRVYSGKPKQVTPLSARTFGTWTLLSAIIRLYAAYNIHNKP 67
 
Name Accession Description Interval E-value
Erg28 pfam03694
Erg28 like protein; This is a family of integral membrane proteins, which may contain four ...
8-75 7.04e-26

Erg28 like protein; This is a family of integral membrane proteins, which may contain four transmembrane helices. Members of this family are thought to be involved in sterol C-4 demethylation. In S. cerevisiae they may tether Erg26p (sterol dehydrogenase/decarboxylase) and Erg27p (3-ketoreductase) to the endoplasmic reticulum or may facilitate interaction between these proteins. The family contains a conserved arginine and histidine that may be functionally important.


Pssm-ID: 461015  Cd Length: 111  Bit Score: 91.79  E-value: 7.04e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343871178   8 LRSWLVMVSIIAMGNTLQSFRdHTFLYEKLYTGKPNLVNGLQARTFGIWTLLSSVIRCLCAIDIHNKT 75
Cdd:pfam03694   1 LPYWLLFVSVVALGNSVQNYF-TLFLTRRVYSGKPKQVTPLSARTFGTWTLLSAIIRLYAAYNIHNKP 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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